PHYSIOLOGICAL VARIANT OF ANTITHROMBIN-III LACKS CARBOHYDRATE SIDE-CHAIN AT ASN-135
PHYSIOLOGICAL VARIANT OF ANTITHROMBIN-III LACKS CARBOHYDRATE SIDE-CHAIN AT ASN-135
复制标题
DOI：
10.1016/0014-5793(87)80266-1
复制
发表时间：
1987-07-27
期刊：
影响因子：
3.5
通讯作者：
JORDAN, RE
中科院分区：
文献类型：
--
作者：
BRENNAN, SO;GEORGE, PM;JORDAN, RE
从混合人血浆中分离出正常抗凝血酶-Ⅲ(AT-Ⅲα)和高亲和力肝素形式(AT-Ⅲβ)。AT-Ⅲβ的负电荷和相对分子质量均低于AT-Ⅲα。唾液酸酶和Endo-F消化表明，固有的差异存在于分子的寡糖成分。CNB片段分析表明，在第104位和第251位残基之间缺少一个寡糖侧链，胰酶消化表明AT-Ⅲβ中的ASN135没有糖基化。刀豆蛋白A-琼脂糖凝胶对总胰酶的层析证实，抗凝血酶的高肝素亲和力形式在ASN 135处缺少寡糖部分。
Both normal antithrombin‐III (AT‐IIIα) and the high heparin affinity form (AT‐IIIβ) were isolated from pooled human plasma. AT‐IIIβ had a lower negative charge and lower molecular mass than AT‐IIIα. Sialidase and endo‐F digestion indicated that the inherent difference resided in the oligosaccharide component of the molecule. CNBr fragmentation showed there was an oligosaccharide sidechain missing between residues 104 and 251, subdigestion with trypsin indicated that Asn 135 was not glycosylated in AT‐IIIβ. Chromatography of total tryptic digests on concanavalin A‐Sepharose confirmed that the high heparin affinity form of antithrombin lacked an oligosaccharide moiety at Asn 135.